STRINGSTRING
cdoA cdoA yetA yetA aspB aspB cysK cysK yhdR yhdR metC metC mccB mccB ytkP ytkP patB patB coaBC coaBC pepA pepA
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
cdoACysteine dioxygenase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (161 aa)    
Predicted Functional Partners:
yetA
Putative enzyme; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
      
 0.920
aspB
Putative aspartate aminotransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
     
 0.904
cysK
Cysteine synthase; Catalyzes the conversion of O-acetylserine to cysteine. Also acts as a sensor of cysteine availability in the signal transduction pathway modulating CymR activity. When cysteine is present, the pool of O-acetylserine (OAS) is low, which leads to the formation of a CymR- CysK complex and transcriptional repression of the CymR regulon occurs. In the absence of cysteine, the OAS pool is high and the CymR-CysK complex is mostly dissociated, leading to a faster dissociation of CymR from its DNA targets and the lifting of CymR-dependent repression.
     
  0.900
yhdR
Putative aspartate aminotransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
     
  0.900
metC
Cystathionine beta-lyase; Catalyzes the transformation of cystathionine into homocysteine. Also exhibits cysteine desulfhydrase activity in vitro, producing sulfide from cysteine; Belongs to the trans-sulfuration enzymes family.
     
  0.900
mccB
Cystathionine gamma-lyase and homocysteine gamma-lyase for reverse transsulfuration pathway; Catalyzes the conversion of cystathionine to cysteine, and homocysteine to sulfide.
     
  0.900
ytkP
Putative cysteine synthase-like protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
     
  0.900
patB
Promiscuous cystathionine beta-lyase / cysteine desulfhydrase; Catalyzes the transformation of cystathionine to homocysteine. Also exhibits cysteine desulfhydrase activity in vitro, producing sulfide from cysteine; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. MalY/PatB cystathionine beta-lyase subfamily.
     
  0.900
coaBC
Coenzyme A biosynthesis bifunctional protein CoaBC; Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'- phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'- phosphopantotheine; In the C-terminal section; belongs to the PPC synthetase family.
     
  0.800
pepA
Leucyl aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides (By similarity).
     
  0.800
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
Server load: low (26%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.